Activation of integrin function by nanopatterned adhesive interfaces
Activation of integrin function by nanopatterned adhesive interfaces
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DOI：
10.1002/cphc.200301014
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发表时间：
2004-03-19
期刊：
影响因子：
2.9
通讯作者：
Spatz, JP
中科院分区：
文献类型：
--
作者：
Arnold, M;Cavalcanti-Adam, EA;Spatz, JP
为了研究单个整合素的分子排列在细胞粘附中的功能，我们通过使用嵌段共聚物胶束纳米光刻法设计了一种六方密排的刚性模板，即涂覆有环状RGDfK肽的细胞粘附性金纳米点。粘合剂点的直径< 8 nm，这允许每个点结合一种整联蛋白。这些点在界面处以28、58、73和85 nm的间距以高精度定位。分离！73 nm的粘附点之间的结果在有限的细胞附着和扩散，并显着减少了粘着斑和肌动蛋白应力纤维的形成。我们将这些细胞反应归因于受限的整联蛋白聚集，而不是细胞-基质界面中配体分子数量不足，因为由具有密集纳米点和没有纳米点的交替场组成的TM微纳米图案化的微纳米基底确实支持细胞粘附。我们认为，58±73 nm之间的范围是整合素聚集和活化的通用长度尺度，因为这些特性被各种培养细胞所共享。
To study the function behind the molecular arrangement of single integrins in cell adhesion, we designed a hexagonally close-packed rigid template of cell-adhesive gold nanodots coated with cyclic RGDfK peptide by using block-copolymer micelle nanolithography. The diameter of the adhesive dots is< 8 nm, which allows the binding of one integrin per dot. These dots are positioned with high precision at 28, 58, 73, and 85 nm spacing at interfaces. A separation of! 73nm between the adhesive dots results in limited cell attachment and spreading, and dramatically reduces the formation of focal adhesion and actin stress fibers. We attribute these cellular responses to restricted integrin clustering rather than insufficient number of ligand molecules in the cell-matrix interface since™ micronanopatterned∫ substrates consisting of alternating fields with dense and no nanodots do support cell adhesion. We propose that the range between 58±73 nm is a universal length scale for integrin clustering and activation, since these properties are shared by a variety of cultured cells.